2nlu: Difference between revisions
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{{STRUCTURE_2nlu| PDB=2nlu | SCENE= }} | |||
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'''Domain-Swapped Dimer of the PWWP Module of Human Hepatoma-derived Growth Factor''' | '''Domain-Swapped Dimer of the PWWP Module of Human Hepatoma-derived Growth Factor''' | ||
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[[Category: Lee, W T.]] | [[Category: Lee, W T.]] | ||
[[Category: Sue, S C.]] | [[Category: Sue, S C.]] | ||
[[Category: | [[Category: Domain-swapping]] | ||
[[Category: | [[Category: Hath]] | ||
[[Category: | [[Category: Hdgf]] | ||
[[Category: | [[Category: Heparin]] | ||
[[Category: | [[Category: Hhdgf]] | ||
[[Category: | [[Category: Hormone/growth factor complex]] | ||
[[Category: | [[Category: Hrp]] | ||
[[Category: | [[Category: Pwwp]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:37:23 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 09:37, 4 May 2008
Domain-Swapped Dimer of the PWWP Module of Human Hepatoma-derived Growth Factor
OverviewOverview
Hepatoma-derived growth factor (hHDGF)-related proteins (HRPs) comprise a new growth factor family sharing a highly conserved and ordered N-terminal PWWP module (residues 1-100, previously referred to as a HATH domain) and a variable disordered C-terminal domain. We have shown that the PWWP module is responsible for heparin binding and have solved its structure in solution. Here, we show that under physiological conditions, both the PWWP module and hHDGF can form dimers. Surface plasmon resonance (SPR) studies revealed that the PWWP dimer binds to heparin with affinity that is two orders of magnitude higher (K(d)=13 nM) than that of the monomeric PWWP module (K(d)=1.2 microM). The monomer-dimer equilibrium properties and NMR structural data together suggest that the PWWP dimer is formed through a domain-swapping mechanism. The domain-swapped PWWP dimer structures were calculated on the basis of the NMR data. The results show that the two PWWP protomers exchange their N-terminal hairpin to form a domain-swapped dimer. The two monomers in a dimer are linked by the long flexible L2 loops, a feature supported by NMR relaxation data for the monomer and dimer. The enhanced heparin-binding affinity of the dimer can be rationalized in the framework of the dimer structure.
About this StructureAbout this Structure
2NLU is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
PWWP module of human hepatoma-derived growth factor forms a domain-swapped dimer with much higher affinity for heparin., Sue SC, Lee WT, Tien SC, Lee SC, Yu JG, Wu WJ, Wu WG, Huang TH, J Mol Biol. 2007 Mar 23;367(2):456-72. Epub 2007 Jan 9. PMID:17270212 Page seeded by OCA on Sun May 4 09:37:23 2008